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CRYSTALLOGRAPHY (23 journals)

Showing 1 - 20 of 20 Journals sorted alphabetically
Acta Crystallographica Section A: Foundations and Advances     Hybrid Journal   (Followers: 8)
Acta Crystallographica Section B: Structural Science, Crystal Engineering and Materials     Hybrid Journal   (Followers: 6)
Acta Crystallographica Section C: Structural Chemistry     Hybrid Journal   (Followers: 4)
Acta Crystallographica Section D : Biological Crystallography     Hybrid Journal   (Followers: 7)
Acta Crystallographica Section E : Crystallographic Communications     Open Access   (Followers: 3)
Acta Crystallographica Section F: Structural Biology Communications     Hybrid Journal   (Followers: 8)
Crystal Growth & Design     Hybrid Journal   (Followers: 13)
Crystal Research and Technology     Hybrid Journal   (Followers: 6)
Crystallography Reports     Hybrid Journal   (Followers: 2)
Crystallography Reviews     Hybrid Journal   (Followers: 3)
IUCrJ     Open Access  
Journal of Applied Crystallography     Hybrid Journal   (Followers: 7)
Journal of Chemical Crystallography     Hybrid Journal   (Followers: 2)
Journal of Crystal Growth     Hybrid Journal   (Followers: 6)
Liquid Crystals     Hybrid Journal   (Followers: 1)
Liquid Crystals Today     Hybrid Journal   (Followers: 1)
Materials and Devices     Open Access  
Molecular Crystals and Liquid Crystals     Hybrid Journal   (Followers: 1)
Polymer crystallization     Hybrid Journal  
Progress in Crystal Growth and Characterization of Materials     Full-text available via subscription   (Followers: 8)
Similar Journals
Journal Cover
Acta Crystallographica Section F: Structural Biology Communications
Journal Prestige (SJR): 0.592
Citation Impact (citeScore): 1
Number of Followers: 8  
 
  Hybrid Journal Hybrid journal (It can contain Open Access articles)
ISSN (Print) 2053-230X
Published by IUCr Homepage  [10 journals]
  • The crystal structure of DynF from the dynemicin-biosynthesis pathway of
           Micromonospora chersina

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      Authors: Kosgei; A.J., Miller, M.D., Bhardwaj, M., Xu, W., Thorson, J.S., Van Lanen, S.G., Phillips, G.N.
      Abstract: Dynemicin is an enediyne natural product from Micromonospora chersina ATCC53710. Access to the biosynthetic gene cluster of dynemicin has enabled the in vitro study of gene products within the cluster to decipher their roles in assembling this unique molecule. This paper reports the crystal structure of DynF, the gene product of one of the genes within the biosynthetic gene cluster of dynemicin. DynF is revealed to be a dimeric eight-stranded β-barrel structure with palmitic acid bound within a cavity. The presence of palmitic acid suggests that DynF may be involved in binding the precursor polyene heptaene, which is central to the synthesis of the ten-membered ring of the enediyne core.
      Keywords: dynemicin; natural products; biosynthetic gene clusters; enediynes; polyketides; anthraquinone; β-barrel; unknown function; Micromonospora chersina ATCC53710
      Citation: urn:issn:2053-230X
      PubDate: 2022-01-01
      DOI: 10.1107/S2053230X21012322
      Issue No: Vol. 78, No. 1 (2022)
       
  • Cryotrapping peroxide in the active site of human mitochondrial manganese
           superoxide dismutase crystals for neutron diffraction

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      Authors: Azadmanesh; J., Lutz, W.E., Coates, L., Weiss, K.L., Borgstahl, G.E.O.
      Abstract: Structurally identifying the enzymatic intermediates of redox proteins has been elusive due to difficulty in resolving the H atoms involved in catalysis and the susceptibility of ligand complexes to photoreduction from X-rays. Cryotrapping ligands for neutron protein crystallography combines two powerful tools that offer the advantage of directly identifying hydrogen positions in redox-enzyme intermediates without radiolytic perturbation of metal-containing active sites. However, translating cryogenic techniques from X-ray to neutron crystallography is not straightforward due to the large crystal volumes and long data-collection times. Here, methods have been developed to visualize the evasive peroxo complex of manganese superoxide dismutase (MnSOD) so that all atoms, including H atoms, could be visualized. The subsequent cryocooling and ligand-trapping methods resulted in neutron data collection to 2.30 Å resolution. The P6122 crystal form of MnSOD is challenging because it has some of the largest unit-cell dimensions (a = b = 77.8, c = 236.8 Å) ever studied using high-resolution cryo-neutron crystallography. The resulting neutron diffraction data permitted the visualization of a dioxygen species bound to the MnSOD active-site metal that was indicative of successful cryotrapping.
      Keywords: human manganese superoxide dismutase; neutron diffraction; large unit cell; cryotrapping; peroxide
      Citation: urn:issn:2053-230X
      PubDate: 2022-01-01
      DOI: 10.1107/S2053230X21012413
      Issue No: Vol. 78, No. 1 (2022)
       
  • X-ray structure of a human cardiac muscle troponin C/troponin I chimera in
           two crystal forms

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      Authors: Yan; C., Sack, J.S.
      Abstract: The X-ray crystal structure of a human cardiac muscle troponin C/troponin I chimera has been determined in two different crystal forms and shows a conformation of the complex that differs from that previously observed by NMR. The chimera consists of the N-terminal domain of troponin C (cTnC; residues 1–80) fused to the switch region of troponin I (cTnI; residues 138–162). In both crystal forms, the cTnI residues form a six-turn α-helix that lays across the hydrophobic groove of an adjacent cTnC molecule in the crystal structure. In contrast to previous models, the cTnI helix runs in a parallel direction relative to the cTnC groove and completely blocks the calcium desensitizer binding site of the cTnC–cTnI interface.
      Keywords: human cardiac muscle troponin C; troponin C/troponin I chimera; calcium regulation; cardiac muscle contraction
      Citation: urn:issn:2053-230X
      PubDate: 2022-01-01
      DOI: 10.1107/S2053230X21012395
      Issue No: Vol. 78, No. 1 (2022)
       
  • Crystal structure of a putative short-chain dehydrogenase/reductase from
           Paraburkholderia xenovorans

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      Authors: Davidson; J., Nicholas, K., Young, J., Conrady, D.G., Mayclin, S., Subramanian, S., Staker, B.L., Myler, P.J., Asojo, O.A.
      Abstract: Paraburkholderia xenovorans degrades organic wastes, including polychlorinated biphenyls. The atomic structure of a putative dehydrogenase/reductase (SDR) from P. xenovorans (PxSDR) was determined in space group P21 at a resolution of 1.45 Å. PxSDR shares less than 37% sequence identity with any known structure and assembles as a prototypical SDR tetramer. As expected, there is some conformational flexibility and difference in the substrate-binding cavity, which explains the substrate specificity. Uniquely, the cofactor-binding cavity of PxSDR is not well conserved and differs from those of other SDRs. PxSDR has an additional seven amino acids that form an additional unique loop within the cofactor-binding cavity. Further studies are required to determine how these differences affect the enzymatic functions of the SDR.
      Keywords: SSGCID; structural genomics; Paraburkholderia xenovorans; oxidoreductases; education and training; detoxification; Seattle Structural Genomics Center for Infectious Disease
      Citation: urn:issn:2053-230X
      PubDate: 2022-01-01
      DOI: 10.1107/S2053230X21012632
      Issue No: Vol. 78, No. 1 (2022)
       
  • Crystal structures of FolM alternative dihydrofolate reductase 1 from
           Brucella suis and Brucella canis

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      Authors: Porter; I., Neal, T., Walker, Z., Hayes, D., Fowler, K., Billups, N., Rhoades, A., Smith, C., Smith, K., Staker, B.L., Dranow, D.M., Mayclin, S.J., Subramanian, S., Edwards, T.E., Myler, P.J., Asojo, O.A.
      Abstract: Members of the bacterial genus Brucella cause brucellosis, a zoonotic disease that affects both livestock and wildlife. Brucella are category B infectious agents that can be aerosolized for biological warfare. As part of the structural genomics studies at the Seattle Structural Genomics Center for Infectious Disease (SSGCID), FolM alternative dihydrofolate reductases 1 from Brucella suis and Brucella canis were produced and their structures are reported. The enzymes share ∼95% sequence identity but have less than 33% sequence identity to other homologues with known structure. The structures are prototypical NADPH-dependent short-chain reductases that share their highest tertiary-structural similarity with protozoan pteridine reductases, which are being investigated for rational therapeutic development.
      Keywords: oxidoreductases; short-chain dehydrogenase/reductase family; dihydrofolate reductases; NADPH; Brucella suis; Brucella canis; Seattle Structural Genomics Center for Infectious Disease; SSGCID
      Citation: urn:issn:2053-230X
      PubDate: 2022-01-01
      DOI: 10.1107/S2053230X21013078
      Issue No: Vol. 78, No. 1 (2022)
       
  • Crystallization and low-resolution structure solution of the SALM3–PTPσ
           synaptic adhesion complex

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      Authors: Karki; S., Kajander, T.
      Pages: 39 - 44
      Abstract: Synaptic adhesion molecules are major organizers of the neuronal network and play a crucial role in the regulation of synapse development and maintenance in the brain. Synaptic adhesion-like molecules (SALMs) and leukocyte common antigen-related receptor protein tyrosine phosphatases (LAR-PTPs) are adhesion protein families with established synaptic function. Dysfunction of several synaptic adhesion molecules has been linked to cognitive disorders such as autism spectrum disorders and schizophrenia. A recent study of the binding and complex structure of SALM3 and PTPσ using small-angle X-ray scattering revealed a 2:2 complex similar to that observed for the interaction of human SALM5 and PTPδ. However, the molecular structure of the SALM3–PTPσ complex remains to be determined beyond the small-angle X-ray scattering model. Here, the expression, purification, crystallization and initial 6.5 Å resolution structure of the mouse SALM3–PTPσ complex are reported, which further verifies the formation of a 2:2 trans-heterotetrameric complex similar to the crystal structure of human SALM5–PTPδ and validates the architecture of the previously reported small-angle scattering-based solution structure of the SALM3–PTPσ complex. Details of the protein expression and purification, crystal optimization trials, and the initial structure solution and data analysis are provided.
      Keywords: synaptic adhesion; SALM3; protein tyrosine phosphatases; protein complex; crystallization
      Citation: urn:issn:2053-230X
      PubDate: 2022-01-01
      DOI: 10.1107/S2053230X21012905
      Issue No: Vol. 78, No. 1 (2022)
       
 
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